Matches in Nanopublications for { ?s ?p "We determined the steady-state kinetic parameters of [Tyr(P)185]ERK2 with respect to the phosphorylation of MBP (Fig.1, Table II). The overall rate of substrate processing (k cat) was ?1000-fold higher than that of [unP]ERK2 and 50-fold lower than that of the fully active [PP]ERK2. The K m value for ATP, which is 12-fold higher in [unP]ERK2 compared with [PP]ERK2, was completely restored by phosphorylation at Tyr185 alone." ?g. }
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- _5 value "We determined the steady-state kinetic parameters of [Tyr(P)185]ERK2 with respect to the phosphorylation of MBP (Fig.1, Table II). The overall rate of substrate processing (k cat) was ?1000-fold higher than that of [unP]ERK2 and 50-fold lower than that of the fully active [PP]ERK2. The K m value for ATP, which is 12-fold higher in [unP]ERK2 compared with [PP]ERK2, was completely restored by phosphorylation at Tyr185 alone." provenance.
- _5 value "We determined the steady-state kinetic parameters of [Tyr(P)185]ERK2 with respect to the phosphorylation of MBP (Fig.1, Table II). The overall rate of substrate processing (k cat) was ?1000-fold higher than that of [unP]ERK2 and 50-fold lower than that of the fully active [PP]ERK2. The K m value for ATP, which is 12-fold higher in [unP]ERK2 compared with [PP]ERK2, was completely restored by phosphorylation at Tyr185 alone." provenance.